HEADER OXIDOREDUCTASE 18-JUL-06 2HQ1
TITLE CRYSTAL STRUCTURE OF ORF 1438 A PUTATIVE GLUCOSE/RIBITOL DEHYDROGENASE
TITLE 2 FROM CLOSTRIDIUM THERMOCELLUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOSE/RIBITOL DEHYDROGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.1.1.62;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM THERMOCELLUM;
SOURCE 3 ORGANISM_TAXID: 1515;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIAL
KEYWDS GLUCOSE/RIBITOL DEHYDROGENASE, CTH-1438, STRUCTURAL GENOMICS,
KEYWDS 2 SOUTHEAST COLLABORATORY FOR STRUCTURAL GENOMICS, SECSG, PSI, PROTEIN
KEYWDS 3 STRUCTURE INITIATIVE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SOUTHEAST COLLABORATORY FOR STRUCTURAL GENOMICS (SECSG),Y.LI,N.SHAW,
AUTHOR 2 H.XU,C.CHENG,L.CHEN,Z.J.LIU,J.P.ROSE,B.C.WANG
REVDAT 4 30-AUG-23 2HQ1 1 REMARK
REVDAT 3 24-JAN-18 2HQ1 1 JRNL
REVDAT 2 24-FEB-09 2HQ1 1 VERSN
REVDAT 1 12-SEP-06 2HQ1 0
JRNL AUTH Y.LI,N.SHAW,H.XU,C.CHENG,L.CHEN,Z.J.LIU,J.P.ROSE,B.C.WANG,
JRNL AUTH 2 SOUTHEAST COLLABORATORY FOR STRUCTURAL GENOMICS
JRNL TITL CRYSTAL STRUCTURE OF ORF 1438 A PUTATIVE GLUCOSE/ RIBITOL
JRNL TITL 2 DEHYDROGENASE FROM CLOSTRIDIUM THERMOCELLUM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.7
REMARK 3 NUMBER OF REFLECTIONS : 19128
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.233
REMARK 3 R VALUE (WORKING SET) : 0.232
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1045
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 927
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 61.95
REMARK 3 BIN R VALUE (WORKING SET) : 0.3120
REMARK 3 BIN FREE R VALUE SET COUNT : 53
REMARK 3 BIN FREE R VALUE : 0.3210
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1535
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 54
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.36000
REMARK 3 B22 (A**2) : 1.90000
REMARK 3 B33 (A**2) : -0.55000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.164
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.143
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.103
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.103
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1566 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2128 ; 1.054 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 223 ; 4.926 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 46 ;40.909 ;26.739
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 249 ;14.363 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 2 ;11.654 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 266 ; 0.066 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1134 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 668 ; 0.181 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1104 ; 0.294 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 60 ; 0.104 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 37 ; 0.151 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.121 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1132 ; 0.542 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1727 ; 0.935 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 499 ; 1.333 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 398 ; 2.035 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2HQ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-06.
REMARK 100 THE DEPOSITION ID IS D_1000038625.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SI CHANNEL 220
REMARK 200 OPTICS : ROSENBAUM
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19128
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.7
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 57.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.35200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.230
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMET
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: PDB ENTRY 1EDO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP VAPOR DIFUSION USING 1
REMARK 280 MICROLITER DROPS CONTAINING EQUAL VOLUMES OF PROTEIN SOLUTION (9
REMARK 280 MG/ML) AND A PRECIPITANT SOLUTION CONTAINING 0.1M AMMONIUM
REMARK 280 DIHYDROGEN PHOSPHATE AND 20% W/V PEG 3350, SETUP AT 291K.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y+1/2,-Z
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 38.99100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.74350
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 38.99100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.74350
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 38.99100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 49.74350
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 38.99100
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 49.74350
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 69.83300
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 -1.000000 0.000000 99.48700
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 99.48700
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 69.83300
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 270 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 92
REMARK 465 ILE A 93
REMARK 465 THR A 94
REMARK 465 ARG A 95
REMARK 465 ASP A 96
REMARK 465 THR A 97
REMARK 465 LEU A 98
REMARK 465 MET A 99
REMARK 465 LEU A 100
REMARK 465 LYS A 101
REMARK 465 MET A 102
REMARK 465 SER A 103
REMARK 465 GLU A 104
REMARK 465 LYS A 105
REMARK 465 ASP A 106
REMARK 465 ILE A 143
REMARK 465 ALA A 144
REMARK 465 GLY A 145
REMARK 465 ILE A 146
REMARK 465 ILE A 147
REMARK 465 GLY A 148
REMARK 465 ASN A 149
REMARK 465 ALA A 150
REMARK 465 GLY A 151
REMARK 465 VAL A 246
REMARK 465 MET A 247
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 4 CG CD CE NZ
REMARK 470 ARG A 15 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 51 CG CD CE NZ
REMARK 470 ASP A 63 CG OD1 OD2
REMARK 470 GLU A 68 CG CD OE1 OE2
REMARK 470 GLU A 71 CG CD OE1 OE2
REMARK 470 TRP A 107 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 107 CZ3 CH2
REMARK 470 ASP A 109 CG OD1 OD2
REMARK 470 VAL A 110 CG1 CG2
REMARK 470 THR A 113 OG1 CG2
REMARK 470 ASN A 114 CG OD1 ND2
REMARK 470 LYS A 116 CG CD CE NZ
REMARK 470 LYS A 123 CG CD CE NZ
REMARK 470 LYS A 127 CG CD CE NZ
REMARK 470 GLN A 152 CG CD OE1 NE2
REMARK 470 ASN A 154 CG OD1 ND2
REMARK 470 TYR A 155 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 MET A 192 CG SD CE
REMARK 470 VAL A 195 CG1 CG2
REMARK 470 ASP A 198 CG OD1 OD2
REMARK 470 LYS A 199 CG CD CE NZ
REMARK 470 VAL A 200 CG1 CG2
REMARK 470 LYS A 201 CG CD CE NZ
REMARK 470 GLU A 202 CG CD OE1 OE2
REMARK 470 MET A 203 CG SD CE
REMARK 470 ASN A 206 CG OD1 ND2
REMARK 470 ASN A 207 CG OD1 ND2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 242 10.73 -141.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CTH-1438 RELATED DB: TARGETDB
DBREF 2HQ1 A 1 247 UNP Q4CFD1 Q4CFD1_CLOTM 1 247
SEQRES 1 A 247 MET GLN LEU LYS GLY LYS THR ALA ILE VAL THR GLY SER
SEQRES 2 A 247 SER ARG GLY LEU GLY LYS ALA ILE ALA TRP LYS LEU GLY
SEQRES 3 A 247 ASN MET GLY ALA ASN ILE VAL LEU ASN GLY SER PRO ALA
SEQRES 4 A 247 SER THR SER LEU ASP ALA THR ALA GLU GLU PHE LYS ALA
SEQRES 5 A 247 ALA GLY ILE ASN VAL VAL VAL ALA LYS GLY ASP VAL LYS
SEQRES 6 A 247 ASN PRO GLU ASP VAL GLU ASN MET VAL LYS THR ALA MET
SEQRES 7 A 247 ASP ALA PHE GLY ARG ILE ASP ILE LEU VAL ASN ASN ALA
SEQRES 8 A 247 GLY ILE THR ARG ASP THR LEU MET LEU LYS MET SER GLU
SEQRES 9 A 247 LYS ASP TRP ASP ASP VAL LEU ASN THR ASN LEU LYS SER
SEQRES 10 A 247 ALA TYR LEU CYS THR LYS ALA VAL SER LYS ILE MET LEU
SEQRES 11 A 247 LYS GLN LYS SER GLY LYS ILE ILE ASN ILE THR SER ILE
SEQRES 12 A 247 ALA GLY ILE ILE GLY ASN ALA GLY GLN ALA ASN TYR ALA
SEQRES 13 A 247 ALA SER LYS ALA GLY LEU ILE GLY PHE THR LYS SER ILE
SEQRES 14 A 247 ALA LYS GLU PHE ALA ALA LYS GLY ILE TYR CYS ASN ALA
SEQRES 15 A 247 VAL ALA PRO GLY ILE ILE LYS THR ASP MET THR ASP VAL
SEQRES 16 A 247 LEU PRO ASP LYS VAL LYS GLU MET TYR LEU ASN ASN ILE
SEQRES 17 A 247 PRO LEU LYS ARG PHE GLY THR PRO GLU GLU VAL ALA ASN
SEQRES 18 A 247 VAL VAL GLY PHE LEU ALA SER ASP ASP SER ASN TYR ILE
SEQRES 19 A 247 THR GLY GLN VAL ILE ASN ILE ASP GLY GLY LEU VAL MET
FORMUL 2 HOH *54(H2 O)
HELIX 1 2 THR A 41 ALA A 53 1 13
HELIX 2 3 ASN A 66 GLY A 82 1 17
HELIX 3 6 GLN A 152 ALA A 174 1 23
HELIX 4 9 THR A 215 SER A 228 1 14
HELIX 5 10 ASP A 229 ASN A 232 5 4
SHEET 1 A 7 VAL A 57 LYS A 61 0
SHEET 2 A 7 ASN A 31 GLY A 36 1 N LEU A 34 O ALA A 60
SHEET 3 A 7 THR A 7 VAL A 10 1 N ALA A 8 O ASN A 31
SHEET 4 A 7 ILE A 86 ASN A 90 1 O VAL A 88 N ILE A 9
SHEET 5 A 7 GLY A 135 ILE A 140 1 O ILE A 140 N ASN A 89
SHEET 6 A 7 ILE A 178 PRO A 185 1 O TYR A 179 N GLY A 135
SHEET 7 A 7 VAL A 238 ILE A 241 1 O ILE A 239 N ALA A 184
CRYST1 77.982 99.487 69.833 90.00 90.00 90.00 C 2 2 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012823 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010052 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014320 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
